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| Hauptseite > Publikationsdatenbank > Ground state structure of D75N mutant of sensory rhodopsin II in complex with its cognate transducer > print |
| Hauptseite > Publikationsdatenbank > Ground state structure of D75N mutant of sensory rhodopsin II in complex with its cognate transducer > print |
| 001 | 202133 | ||
| 005 | 20240610115647.0 | ||
| 024 | 7 | _ | |a 10.1016/j.jphotobiol.2013.03.008 |2 doi |
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| 041 | _ | _ | |a English |
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| 100 | 1 | _ | |a Ishchenko, A. |0 P:(DE-Juel1)131968 |b 0 |
| 245 | _ | _ | |a Ground state structure of D75N mutant of sensory rhodopsin II in complex with its cognate transducer |
| 260 | _ | _ | |a New York, NY [u.a.] |c 2013 |b Elsevier |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1435731696_2489 |2 PUB:(DE-HGF) |
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| 336 | 7 | _ | |a article |2 DRIVER |
| 520 | _ | _ | |a The complex of sensory rhodopsin II (NpSRII) with its cognate transducer (NpHtrII) mediates negative phototaxis in halobacteria Natronomonas pharaonis. Upon light activation NpSRII triggers, by means of NpHtrII, a signal transduction chain homologous to the two component system in eubacterial chemotaxis. Here we report on the crystal structure of the ground state of the mutant NpSRII-D75N/NpHtrII complex in the space group I212121. Mutations of this aspartic acid in light-driven proton pumps dramatically modify or/and inhibit protein functions. However, in vivo studies show that the similar D75N mutation retains functionality of the NpSRII/NpHtrII complex. The structure provides the molecular basis for the explanation of the unexpected observation that the wild and the mutant complexes display identical physiological response on light excitation. |
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| 773 | _ | _ | |a 10.1016/j.jphotobiol.2013.03.008 |g Vol. 123, p. 55 - 58 |0 PERI:(DE-600)1482691-4 |p 55 - 58 |t Journal of photochemistry and photobiology / B |v 123 |y 2013 |x 1011-1344 |
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